Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Small GTPases - Ras and Rho01:24

Small GTPases - Ras and Rho

Ras and Rho are small monomeric GTPases that act downstream of receptor tyrosine kinase (RTK) and regulate various cellular processes. These GTPases switch between active and inactive states by binding to guanine nucleotides.
Three regulatory proteins control their activity:
Rab Cascades01:25

Rab Cascades

Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.
Rab Proteins01:14

Rab Proteins

Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...
GTPases and their Regulation02:14

GTPases and their Regulation

Guanine nucleotide-binding proteins (G-proteins), also known as GTPases, are a superfamily of proteins that regulate many cellular processes, such as cell signaling, vesicular transport, and the regulation of cell shape and motility. Mutation or dysfunction of these proteins can lead to disease. There are around 40,000 known G-proteins that can broadly be classified into two groups ‒  small G-proteins consisting of a single domain and large multi-domain G-proteins.
Large G-proteins, also known...
GTPases and their Regulation02:14

GTPases and their Regulation

Guanine nucleotide-binding proteins (G-proteins), also known as GTPases, are a superfamily of proteins that regulate many cellular processes, such as cell signaling, vesicular transport, and the regulation of cell shape and motility. Mutation or dysfunction of these proteins can lead to disease. There are around 40,000 known G-proteins that can broadly be classified into two groups ‒  small G-proteins consisting of a single domain and large multi-domain G-proteins.
Large G-proteins, also known...
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Endosome maturation is orchestrated by inside-out proton signaling through a Na<sup>+</sup>/H<sup>+</sup> exchanger and pH-dependent Rab GTPase cycling.

Nature communications·2026
Same author

Endosome maturation is orchestrated by inside-out proton signaling through a Na+/H+ exchanger and pH-dependent Rab GTPase cycling.

bioRxiv : the preprint server for biology·2025
Same author

Systems-level effects of allosteric perturbations to a model molecular switch.

Nature·2021
Same author

High-Throughput Assay for Profiling the Substrate Specificity of Rab GTPase-Activating Proteins.

Methods in molecular biology (Clifton, N.J.)·2021
Same author

Propelling COPII vesicle biogenesis at the endoplasmic reticulum.

Structure (London, England : 1993)·2021
Same author

Molecular basis for KDEL-mediated retrieval of escaped ER-resident proteins - SWEET talking the COPs.

Journal of cell science·2020
Same journal

Mechanosensing in immune cells: Implications for migration and beyond.

Current opinion in cell biology·2026
Same journal

Emerging role of organelles in cell migration.

Current opinion in cell biology·2026
Same journal

Nuclear adaptation in cell migration.

Current opinion in cell biology·2026
Same journal

Patterns in motion: Choreographing dynamic cell behaviours during tissue repair.

Current opinion in cell biology·2026
Same journal

Quo vadis reconstituted cell surfaces? Purpose and future perspectives for minimal systems of the cell plasma membrane.

Current opinion in cell biology·2026
Same journal

Nuclear determinants of mRNA and protein isoforms.

Current opinion in cell biology·2026
See all related articles

Related Experiment Video

Updated: Jun 13, 2026

Affinity Precipitation of Active Rho-GEFs Using a GST-tagged Mutant Rho Protein (GST-RhoA(G17A)) from Epithelial Cell Lysates
11:28

Affinity Precipitation of Active Rho-GEFs Using a GST-tagged Mutant Rho Protein (GST-RhoA(G17A)) from Epithelial Cell Lysates

Published on: March 31, 2012

Rab GEFs and GAPs.

Francis Barr1, David G Lambright

  • 1University of Liverpool, Cancer Research Centre, 200 London Road, Liverpool L3 9TA, UK. fabarr@liverpool.ac.uk

Current Opinion in Cell Biology
|May 15, 2010
PubMed
Summary
This summary is machine-generated.

Rab GTPases regulate membrane trafficking and are controlled by GDP-GTP exchange factors (GEFs) and GTP-hydrolysis activating proteins (GAPs). Recent studies reveal new insights into their mechanisms and cellular roles.

More Related Videos

Capturing Common Fragile Site Breaks by Native &#947;H2A.X ChIP
09:46

Capturing Common Fragile Site Breaks by Native γH2A.X ChIP

Published on: January 24, 2025

A G-quadruplex DNA-affinity Approach for Purification of Enzymatically Active G4 Resolvase1
11:25

A G-quadruplex DNA-affinity Approach for Purification of Enzymatically Active G4 Resolvase1

Published on: March 18, 2017

Related Experiment Videos

Last Updated: Jun 13, 2026

Affinity Precipitation of Active Rho-GEFs Using a GST-tagged Mutant Rho Protein (GST-RhoA(G17A)) from Epithelial Cell Lysates
11:28

Affinity Precipitation of Active Rho-GEFs Using a GST-tagged Mutant Rho Protein (GST-RhoA(G17A)) from Epithelial Cell Lysates

Published on: March 31, 2012

Capturing Common Fragile Site Breaks by Native &#947;H2A.X ChIP
09:46

Capturing Common Fragile Site Breaks by Native γH2A.X ChIP

Published on: January 24, 2025

A G-quadruplex DNA-affinity Approach for Purification of Enzymatically Active G4 Resolvase1
11:25

A G-quadruplex DNA-affinity Approach for Purification of Enzymatically Active G4 Resolvase1

Published on: March 18, 2017

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Rab proteins are GTP-binding proteins crucial for membrane trafficking.
  • Their activity is tightly regulated by GDP-GTP exchange factors (GEFs) and GTP-hydrolysis activating proteins (GAPs).
  • GAPs often contain a conserved TBC domain, suggesting a common regulatory mechanism.

Purpose of the Study:

  • To elucidate the mechanisms underlying Rab GDP-GTP exchange factor (GEF) and GTP-hydrolysis activating protein (GAP) action.
  • To understand the roles of these regulatory proteins in cellular trafficking pathways.
  • To integrate recent structural and cell biological findings into a cohesive view of Rab regulation.

Main Methods:

  • Review and synthesis of recent structural biology studies.
  • Analysis of cell biological data on Rab protein function.
  • Integration of findings on Rab GEF and GAP mechanisms.

Main Results:

  • New structural and cell biological data provide detailed insights into how GEFs and GAPs modulate Rab GTPase activity.
  • The diverse GEF families and the TBC-domain-containing GAPs employ distinct mechanisms to regulate specific Rab proteins.
  • These regulatory events are critical for orchestrating various cellular trafficking pathways.

Conclusions:

  • Recent advances have significantly improved our understanding of Rab regulatory mechanisms.
  • The interplay between Rabs, GEFs, and GAPs is fundamental for precise control of membrane trafficking.
  • Further research into these pathways will illuminate fundamental cellular processes and potential therapeutic targets.